Inhibition of Porcine Pancreatic Elastase by 7-Substituted 4-Chloro-3-Ethoxyisocoumarins: Structural Characteristics of Modeled Noncovalent Complexes Relate to the Measured Inhibition Kinetics

Kinetic measurements for the inhibition of porcine pancreatic elastase by 7-substituted 4-chloro-.3-ethox-yisocoumarins were performed. To obtain possible explanations for the kinetic results, structures resulting from energy minimizations of inhibitor-enzyme complex structures where each inhibitor...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1993-02, Vol.300 (2), p.588-597
Hauptverfasser:	Plaskon, R.R., Kam, C.M., Kerrigan, J.E., Burgess, E.M., Powers, J.C., Suddath, F.L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Coumarins - chemistry Coumarins - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Kinetics Molecular Conformation Pancreas - enzymology Pancreatic Elastase - antagonists & inhibitors Pancreatic Elastase - chemistry Protein Conformation Structure-Activity Relationship Swine
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